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Overview
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The HSPA1B Protein Human produced in E. Coli is a single, non-glycosylated polypeptide chain containing 650 amino acids having a molecular mass of 71.16kDa. HSPA1B is fused to a 10 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques. The HSP70 family is found in many intracellular compartments such as chloroplasts, endoplasmic reticulum, mitochondria, and cytosol. These proteins are induced by a variation of biological stresses, including heat stress, in every organism. HSP70 has a range of functions. For example: HSP70 acts as molecular chaperones facilitating the assembly of multi-protein complexes, HSP70 take part in the translocation of polypeptides across cell membranes and to the nucleus, and HSP70 assists in the proper folding of nascent polypeptide chains. HSP70 is a mitochondrial import equipment and has a crucial part in the cytosolic endoplasmic reticulum. Lately, extracellular localized HSP was discovered to take an important part in the induction of a cellular immune response.
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- Properties
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Overview